Literature DB >> 6480818

The rate of polymerization of rabbit skeletal muscle actin is enhanced by polyethylene glycol.

M Strömqvist, L Backman, V P Shanbhag.   

Abstract

The effect of polyethylene glycol on the kinetics of actin polymerization was determined by monitoring the enhancement in the fluorescence of pyrenyl-labelled actin. The polymerization of actin at 15 mM KCl was in addition followed by viscometry and light scattering. All three methods showed that the overall rate of polymerization of actin increased 3-4-fold when the concentration of polyethylene glycol was increased from 0 to 6% (ww-1). A further increase in polyethylene glycol concentration to 10% (ww-1) caused a relatively small contribution to the increase in the rate of polymerization. The enhancement of the overall rate of polymerization by polyethylene glycol was also reflected in a significant decrease in the lag time observed when the time course of polymerization was followed by viscometry and light scattering. The steady-state value of fluorescence enhancement and critical concentration of actin were also influenced by polyethylene glycol and the results showed that the extent of polymerization was increased by an increase in the concentration of polyethylene glycol in solution. The effect of polyethylene glycol on both rate and extent of polymerization persisted at physiological salt concentration (150 mM KCl, 2 mM MgCl2). Since the rate of elongation was affected only to a small extent by polyethylene glycol, we propose that its main effect is on nucleation.

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Year:  1984        PMID: 6480818     DOI: 10.1007/bf00818262

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  20 in total

1.  Physiological function of connective tissue polysaccharides.

Authors:  W D Comper; T C Laurent
Journal:  Physiol Rev       Date:  1978-01       Impact factor: 37.312

2.  Structure and circular dichroism of DNA in concentrated polymer solutions.

Authors:  C F Jordan; L S Lerman; J H Venable
Journal:  Nat New Biol       Date:  1972-03-22

3.  Complete amino-acid sequence of actin of rabbit skeletal muscle.

Authors:  M Elzinga; J H Collins; W M Kuehl; R S Adelstein
Journal:  Proc Natl Acad Sci U S A       Date:  1973-09       Impact factor: 11.205

4.  Enzyme reactions in polymer media.

Authors:  T C Laurent
Journal:  Eur J Biochem       Date:  1971-08-25

5.  Thermodynamical aspect of G-F transformations of actin.

Authors:  M Kasai
Journal:  Biochim Biophys Acta       Date:  1969-06-24

6.  The depolymerization of actin by specific proteins from plasma and brain: a quantitative assay.

Authors:  H E Harris; J R Bamburg; B W Bernstein; A G Weeds
Journal:  Anal Biochem       Date:  1982-01-01       Impact factor: 3.365

7.  Polymerization-induced changes in the fluorescence of actin labeled with iodoacetamidotetramethylrhodamine.

Authors:  J F Tait; C Frieden
Journal:  Arch Biochem Biophys       Date:  1982-06       Impact factor: 4.013

8.  Mechanism of action of phalloidin on the polymerization of muscle actin.

Authors:  J E Estes; L A Selden; L C Gershman
Journal:  Biochemistry       Date:  1981-02-17       Impact factor: 3.162

9.  Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures.

Authors:  K Gekko; S N Timasheff
Journal:  Biochemistry       Date:  1981-08-04       Impact factor: 3.162

10.  Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.

Authors:  T Spector
Journal:  Anal Biochem       Date:  1978-05       Impact factor: 3.365

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